Journal article
Modulation of the substrate specificity of the kinase PDK1 by distinct conformations of the full-length protein
- Abstract:
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The activation of at least 23 different mammalian kinases requires the phosphorylation of their hydrophobic motifs by the kinase PDK1. A linker connects the phosphoinositide-binding PH domain to the catalytic domain, which contains a docking site for substrates called the PIF pocket. Here, we used a chemical biology approach to show that PDK1 existed in equilibrium between at least three distinct conformations with differing substrate specificities. The inositol polyphosphate derivative HYG8 ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Access Document
- Files:
-
-
(Preview, Accepted manuscript, pdf, 12.3MB, Terms of use)
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- Publisher copy:
- 10.1126/scisignal.add3184
Authors
Funding
Bibliographic Details
- Publisher:
- American Association for the Advancement of Science
- Journal:
- Science Signaling More from this journal
- Volume:
- 16
- Issue:
- 789
- Article number:
- eadd3184
- Publication date:
- 2023-06-13
- Acceptance date:
- 2023-05-19
- DOI:
- EISSN:
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1937-9145
- ISSN:
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1945-0877
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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1392454
- Local pid:
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pubs:1392454
- Deposit date:
-
2023-06-12
Terms of use
- Copyright holder:
- Sacerdoti et al
- Copyright date:
- 2023
- Rights statement:
- © 2023 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
- Notes:
- For the purpose of Open Access, the authors have applied a CC BY public copyright licence to any Author Accepted Manuscript version arising from this submission. This is the accepted manuscript version of the article. The final version is available online from AAAS at: https://doi.org/10.1126/scisignal.add3184
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